Publication: Histochemical study of expression of lectin-reactive carbohydrate epitopes and glycoligand-binding sites in normal human appendix vermiformis, colonic mucosa,
acute appendicitis and colonic adenoma
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Date
1996
Authors
Brinck, U. ; Bosbach, R. ; Korabiowska, M. ; Schauer, A. ; Gabius, H.J.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
In a glycohistochemical analysis of human
appendix vermiformis we report the assessment of lectin
binding in cells of the Gut Associated Lymphoid Tissue
of normal samples and in acute appendicitis using a
panel of plant, invertebrate and mammalian lectins with
specificity for a-L-Fuc (UEA-I), a-D-Gluc and a-DMan
(Con A), a-D-GalNAc (DBA), GalNAc (SBA,
HPA), B-Gal (RCA-I, 14 kDa=galectin-l) and a-, B-Gal
(VAA). Moreover, we initiate the study of expression of
carbohydrate-binding sites in this tissue and in colonic
mucosa, employing several types of carrier-immobilized
carbohydrate ligands as suitable probes for this purpose.
Within the three populations of macrophages intralsubepithelial
macrophages of the dome region, the
lamina propria of the intercryptal region and the follicleassociated
epithelium were apparently reactive with
most of the lectins and also with mannose and fucose
residues of the tested neoglycoproteins. Distinguishing
features of germinal center macrophages in relation to
intra-/subepithelia1 phagocytes were the lack of binding
of UEA-I and DBA. In comparison to all other types of
phagocytes, macrophages of the T-region displayed a
rather restricted binding capacity only to Con A and
RCA-I. Labeling of macrophages with SBA, HPA and
VAA in this location was only rarely found. With respect
to dendritic cells no consistently positive reaction was
seen for follicular cells, whereas interdigitating cells of
the T-region bound Con A, HPA and RCA-I, and, less
frequently, SBA.
Lymphocytes in all anatomical subsites of the Gut
Associated Lymphoid Tissue, centrocytes, centroblasts and plasma cells had binding sites for Con A and RCA-I
in common. Notably, a small number of lymphocytes
mostly in the T-region but also in B-cell-rich areas expressed intranuclear binding sites for fucose and
mannose residues. Intraepithelial lymphocytes and
lymphatic cells of the T-region differed from lymphocytes
in other regions by a more frequent expression of
VAA-binding sites.
The epithelium of appendix vermiformis and colonic
mucosa not only presents lectin binding sites, but also
has the capacity to bind carbohydrate structures, as
shown by labeled glycoligand-exposing neoglycoproteins.
In normal mucosa the extent of binding
appeared to be associated with maturation of cells, the
surface epithelium showing the most intense staining
reaction. This pattern is not detectable in colonic
adenoma which reveal increased intensity, when
compared to normal mucosa. In contrast to development
of hyperplasia, acute inflammation in appendicitis
caused no detectable changes of neoglycoprotein
binding. Taking our previous assessment on lectin
binding in appendicitis into account, we conclude that
glycosylation of goblet cell mucus, but not the capacity
to bind certain sugar epitopes responds to inflammatory
processes, whereas tumorigenesis of colonic adenoma
can also affect the binding of neoglycoproteins.
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